메뉴 건너뛰기




Volumn 113, Issue 10, 2011, Pages 1207-1218

Cytotoxic complexes of sodium oleate with β-lactoglobulin

Author keywords

Lactoglobulin; Apoptosis; Cytotoxicity; Denaturation and aggregation; Oleate

Indexed keywords

BOVINAE; RATTUS;

EID: 80054104652     PISSN: 14387697     EISSN: 14389312     Source Type: Journal    
DOI: 10.1002/ejlt.201100109     Document Type: Article
Times cited : (50)

References (60)
  • 2
    • 31444454246 scopus 로고    scopus 로고
    • Roginski, H., Fuquay, J. W., Fox, P. F. (Eds.), Academic Press, London
    • Creamer, L. K., Sawyer, L., in: Roginski, H., Fuquay, J. W., Fox, P. F. (Eds.), Encyclopedia of Dairy Sciences, Academic Press, London 2003.
    • (2003) Encyclopedia of Dairy Sciences
    • Creamer, L.K.1    Sawyer, L.2
  • 3
    • 0021876620 scopus 로고
    • Homology of beta-lactoglobulin, serum retinol-binding protein, and protein HC
    • Pervaiz, S., Brew, K., Homology of beta-lactoglobulin, serum retinol-binding protein, and protein HC. Science 1985, 228, 335-337.
    • (1985) Science , vol.228 , pp. 335-337
    • Pervaiz, S.1    Brew, K.2
  • 4
    • 0022931198 scopus 로고
    • The structure of beta-lactoglobulin and its similarity to plasma retinol-binding protein
    • Papiz, M. Z., Sawyer, L., Eliopoulos, E. E., North, A. C. et al., The structure of beta-lactoglobulin and its similarity to plasma retinol-binding protein. Nature 1986, 324, 383-385.
    • (1986) Nature , vol.324 , pp. 383-385
    • Papiz, M.Z.1    Sawyer, L.2    Eliopoulos, E.E.3    North, A.C.4
  • 5
    • 0029790266 scopus 로고    scopus 로고
    • The lipocalin protein family: Structure and function
    • Flower, D. R., The lipocalin protein family: Structure and function. Biochem. J. 1996, 318, 1-14.
    • (1996) Biochem. J. , vol.318 , pp. 1-14
    • Flower, D.R.1
  • 6
    • 0014770081 scopus 로고
    • Binding of long chain fatty acids to beta-lactoglobulin
    • Spector, A. A., Fletcher, J. E., Binding of long chain fatty acids to beta-lactoglobulin. Lipids 1970, 5, 403-411.
    • (1970) Lipids , vol.5 , pp. 403-411
    • Spector, A.A.1    Fletcher, J.E.2
  • 7
    • 0024815231 scopus 로고
    • Interaction of fatty acids with beta-lactoglobulin and albumin from ruminant milk
    • Pérez, M. D., de Villegas, C. D., Sánchez, L., Aranda, P. et al., Interaction of fatty acids with beta-lactoglobulin and albumin from ruminant milk. J. Biochem. 1989, 106, 1094-1097.
    • (1989) J. Biochem. , vol.106 , pp. 1094-1097
    • Pérez, M.D.1    de Villegas, C.D.2    Sánchez, L.3    Aranda, P.4
  • 8
    • 84887346615 scopus 로고
    • Interaction of bovine-lactoglobulin and other bovine and human whey proteins with retinol and fatty acids
    • Puyol, P., Perez, M. D., Ena, J. M., Calvo, M., Interaction of bovine-lactoglobulin and other bovine and human whey proteins with retinol and fatty acids. Agric. Biol. Chem. 1991, 55, 2515-2520.
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 2515-2520
    • Puyol, P.1    Perez, M.D.2    Ena, J.M.3    Calvo, M.4
  • 9
    • 0035160316 scopus 로고    scopus 로고
    • A folding variant of human alpha-lactalbumin induces mitochondrial permeability transition in isolated mitochondria
    • Kohler, C., Gogvadze, V., Hakansson, A., Svanborg, C. et al., A folding variant of human alpha-lactalbumin induces mitochondrial permeability transition in isolated mitochondria. Eur. J. Biochem. 2001, 268, 186-191.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 186-191
    • Kohler, C.1    Gogvadze, V.2    Hakansson, A.3    Svanborg, C.4
  • 11
    • 18344368870 scopus 로고    scopus 로고
    • HAMLET kills tumor cells by apoptosis: Structure, cellular mechanisms, and therapy
    • Gustafsson, L., Hallgren, O., Mossberg, A. K., Pettersson, J. et al., HAMLET kills tumor cells by apoptosis: Structure, cellular mechanisms, and therapy. J. Nutr. 2005, 135, 1299-1303.
    • (2005) J. Nutr. , vol.135 , pp. 1299-1303
    • Gustafsson, L.1    Hallgren, O.2    Mossberg, A.K.3    Pettersson, J.4
  • 13
    • 58749114573 scopus 로고    scopus 로고
    • HAMLET (human alpha-lactalbumin made lethal to tumor cells) triggers autophagic tumor cell death
    • Aits, S., Gustafsson, L., Hallgren, O., Brest, P. et al., HAMLET (human alpha-lactalbumin made lethal to tumor cells) triggers autophagic tumor cell death. Int. J. Cancer 2009, 124, 1008-1019.
    • (2009) Int. J. Cancer , vol.124 , pp. 1008-1019
    • Aits, S.1    Gustafsson, L.2    Hallgren, O.3    Brest, P.4
  • 16
    • 10744223979 scopus 로고    scopus 로고
    • Alpha-Lactalbumin unfolding is not sufficient to cause apoptosis, but is required for the conversion to HAMLET (human alpha-lactalbumin made lethal to tumor cells)
    • Svensson, M., Fast, J., Mossberg, A., Kristin, Duringer, C., Gustafsson, L., Hallgren, O., et al., Alpha-Lactalbumin unfolding is not sufficient to cause apoptosis, but is required for the conversion to HAMLET (human alpha-lactalbumin made lethal to tumor cells). Protein Sci. 2003, 12, 2794-2804.
    • (2003) Protein Sci. , vol.12 , pp. 2794-2804
    • Svensson, M.1    Fast, J.2    Mossberg, A.3    Kristin4    Duringer, C.5    Gustafsson, L.6    Hallgren, O.7
  • 17
    • 33646386189 scopus 로고    scopus 로고
    • Alpha-lactalbumin species variation, HAMLET formation, and tumor cell death
    • Pettersson, J., Mossberg, A.-K., Svanborg, C., Alpha-lactalbumin species variation, HAMLET formation, and tumor cell death. Biochem. Biophys. Res. Commun. 2006, 345, 260-270.
    • (2006) Biochem. Biophys. Res. Commun. , vol.345 , pp. 260-270
    • Pettersson, J.1    Mossberg, A.-K.2    Svanborg, C.3
  • 18
    • 68149162285 scopus 로고    scopus 로고
    • Protein oligomerization induced by oleic acid at the solid-liquid interface - equine lysozyme cytotoxic complexes
    • Wilhelm, K., Darinskas, A., Noppe, W., Duchardt, E. et al., Protein oligomerization induced by oleic acid at the solid-liquid interface - equine lysozyme cytotoxic complexes. FEBS J. 2009, 276, 3975-3989.
    • (2009) FEBS J. , vol.276 , pp. 3975-3989
    • Wilhelm, K.1    Darinskas, A.2    Noppe, W.3    Duchardt, E.4
  • 19
    • 0024328847 scopus 로고
    • Refined structure of baboon alpha-lactalbumin at 1.7 A resolution. Comparison with C-type lysozyme
    • Acharya, K. R., Stuart, D. I., Walker, N. P., Lewis, M., Phillips, D. C., Refined structure of baboon alpha-lactalbumin at 1.7 A resolution. Comparison with C-type lysozyme. J. Mol. Biol. 1989, 208, 99-127.
    • (1989) J. Mol. Biol. , vol.208 , pp. 99-127
    • Acharya, K.R.1    Stuart, D.I.2    Walker, N.P.3    Lewis, M.4    Phillips, D.C.5
  • 20
    • 0025811817 scopus 로고
    • Lysozyme and alpha-lactalbumin: Structure, function, and interrelationships
    • McKenzie, H. A., White, F. H., Jr., Lysozyme and alpha-lactalbumin: Structure, function, and interrelationships. Adv. Protein Chem. 1991, 41, 173-315.
    • (1991) Adv. Protein Chem. , vol.41 , pp. 173-315
    • McKenzie, H.A.1    White Jr., F.H.2
  • 21
    • 0030800608 scopus 로고    scopus 로고
    • Molecular divergence of lysozymes and alpha-lactalbumin
    • Qasba, P. K., Kumar, S., Molecular divergence of lysozymes and alpha-lactalbumin. Crit. Rev. Biochem. Mol. Biol. 1997, 32, 255-306.
    • (1997) Crit. Rev. Biochem. Mol. Biol. , vol.32 , pp. 255-306
    • Qasba, P.K.1    Kumar, S.2
  • 22
    • 0036891687 scopus 로고    scopus 로고
    • Partly folded states of members of the lysozyme/lactalbumin superfamily: A comparative study by circular dichroism spectroscopy and limited proteolysis
    • Polverino de. Laureto, P., Frare, E., Gottardo, R., Van Dael, H., Fontana, A., Partly folded states of members of the lysozyme/lactalbumin superfamily: A comparative study by circular dichroism spectroscopy and limited proteolysis. Protein Sci. 2002, 11, 2932-2946.
    • (2002) Protein Sci. , vol.11 , pp. 2932-2946
    • Polverino de. Laureto, P.1    Frare, E.2    Gottardo, R.3    Van Dael, H.4    Fontana, A.5
  • 23
    • 1542405871 scopus 로고    scopus 로고
    • Human alpha-lactalbumin made lethal to tumor cells (HAMLET) kills human glioblastoma cells in brain xenografts by an apoptosis-like mechanism and prolongs survival
    • Fischer, W., Gustafsson, L., Mossberg, A. K., Gronli, J. et al., Human alpha-lactalbumin made lethal to tumor cells (HAMLET) kills human glioblastoma cells in brain xenografts by an apoptosis-like mechanism and prolongs survival. Cancer Res. 2004, 64, 2105-2112.
    • (2004) Cancer Res. , vol.64 , pp. 2105-2112
    • Fischer, W.1    Gustafsson, L.2    Mossberg, A.K.3    Gronli, J.4
  • 26
    • 34548073069 scopus 로고    scopus 로고
    • Bladder cancers respond to intravesical instillation of (HAMLET human alpha-lactalbumin made lethal to tumor cells)
    • Mossberg, A. K., Wullt, B., Gustafsson, L., Mansson, W., Ljunggren, E., Svanborg, C., Bladder cancers respond to intravesical instillation of (HAMLET human alpha-lactalbumin made lethal to tumor cells). Int. J. Cancer 2007, 121, 1352-1359.
    • (2007) Int. J. Cancer , vol.121 , pp. 1352-1359
    • Mossberg, A.K.1    Wullt, B.2    Gustafsson, L.3    Mansson, W.4    Ljunggren, E.5    Svanborg, C.6
  • 27
    • 77950648249 scopus 로고    scopus 로고
    • Effect of denaturation of alpha-lactalbumin on the formation of BAMLET (bovine alpha-lactalbumin made lethal to tumor cells)
    • Lišková, K., Kelly, A. L., O'Brien, N., Brodkorb, A., Effect of denaturation of alpha-lactalbumin on the formation of BAMLET (bovine alpha-lactalbumin made lethal to tumor cells). J. Agric. Food Chem. 2010, 58, 4421-4427.
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 4421-4427
    • Lišková, K.1    Kelly, A.L.2    O'Brien, N.3    Brodkorb, A.4
  • 28
    • 84861096921 scopus 로고    scopus 로고
    • Ireland Patent WO2010131237 (A1)
    • Brodkorb, A., Lišková, K., Ireland Patent WO2010131237 (A1), 2010.
    • (2010)
    • Brodkorb, A.1    Lišková, K.2
  • 30
    • 1942441014 scopus 로고    scopus 로고
    • Spectroscopic characterization of heat-induced nonnative beta-lactoglobulin monomers
    • Croguennec, T., Molle, D., Mehra, R., Bouhallab, S., Spectroscopic characterization of heat-induced nonnative beta-lactoglobulin monomers. Protein Sci. 2004, 13, 1340-1346.
    • (2004) Protein Sci. , vol.13 , pp. 1340-1346
    • Croguennec, T.1    Molle, D.2    Mehra, R.3    Bouhallab, S.4
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 80053892501 scopus 로고    scopus 로고
    • Formation of non-native β-lactoglobulin during heat-induced denaturation
    • DOI: 10.1007/s11483-011-9230-3
    • Kehoe, J. J., Wang, L., Morris, E. R., Brodkorb, A., Formation of non-native β-lactoglobulin during heat-induced denaturation. Food Biophys. 2011, DOI: 10.1007/s11483-011-9230-3.
    • (2011) Food Biophys.
    • Kehoe, J.J.1    Wang, L.2    Morris, E.R.3    Brodkorb, A.4
  • 33
    • 84916555996 scopus 로고
    • Effect of binding of retinol and palmitic acid to bovine {beta}-lactoglobulin on its resistance to thermal denaturation
    • Puyol, P., Perez, M. D., Peiro, J. M., Calvo, M., Effect of binding of retinol and palmitic acid to bovine {beta}-lactoglobulin on its resistance to thermal denaturation. J. Dairy Sci. 1994, 77, 1494-1502.
    • (1994) J. Dairy Sci. , vol.77 , pp. 1494-1502
    • Puyol, P.1    Perez, M.D.2    Peiro, J.M.3    Calvo, M.4
  • 34
    • 0032003930 scopus 로고    scopus 로고
    • Effect of the binding of palmitic acid to [beta]-lactoglobulin on its gelation properties
    • Puyol, P., Pérez, M. D., Burgos, J., Calvo, M., Effect of the binding of palmitic acid to [beta]-lactoglobulin on its gelation properties. Int. Dairy J. 1998, 8, 119-123.
    • (1998) Int. Dairy J. , vol.8 , pp. 119-123
    • Puyol, P.1    Pérez, M.D.2    Burgos, J.3    Calvo, M.4
  • 35
    • 0028567981 scopus 로고
    • A model for the denaturation and aggregation of beta-lactoglobulin
    • Roefs, S. P., De Kruif, K. G., A model for the denaturation and aggregation of beta-lactoglobulin. Eur. J. Biochem./FEBS 1994, 226, 883-889.
    • (1994) Eur. J. Biochem./FEBS , vol.226 , pp. 883-889
    • Roefs, S.P.1    De Kruif, K.G.2
  • 36
    • 34548295724 scopus 로고    scopus 로고
    • Determination of exposed sulphydryl groups in heated β-lactoglobulin A using IAEDANS and mass spectrometry
    • Kehoe, J. J., Brodkorb, A., Molle, D., Yokoyama, E. et al., Determination of exposed sulphydryl groups in heated β-lactoglobulin A using IAEDANS and mass spectrometry. J. Agric. Food Chem. 2007, 55, 7107-7113.
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 7107-7113
    • Kehoe, J.J.1    Brodkorb, A.2    Molle, D.3    Yokoyama, E.4
  • 37
    • 1542575976 scopus 로고    scopus 로고
    • Heat-induced denaturation/aggregation of beta-lactoglobulin A and B: Kinetics of the first intermediates formed
    • Croguennec, T., O'Kennedy, B. T., Mehra, R., Heat-induced denaturation/aggregation of beta-lactoglobulin A and B: Kinetics of the first intermediates formed. Int. Dairy J. 2004, 14, 399-409.
    • (2004) Int. Dairy J. , vol.14 , pp. 399-409
    • Croguennec, T.1    O'Kennedy, B.T.2    Mehra, R.3
  • 38
    • 77951767673 scopus 로고    scopus 로고
    • The interaction of equine lysozyme:oleic acid complexes with lipid membranes suggests a cargo off-loading mechanism
    • Nielsen, S. B., Wilhelm, K., Vad, B., Schleucher, J. et al., The interaction of equine lysozyme:oleic acid complexes with lipid membranes suggests a cargo off-loading mechanism. J. Mol. Biol. 2010, 398, 351-361.
    • (2010) J. Mol. Biol. , vol.398 , pp. 351-361
    • Nielsen, S.B.1    Wilhelm, K.2    Vad, B.3    Schleucher, J.4
  • 39
    • 0027578704 scopus 로고
    • Reversible effects of medium dielectric constant on structural transformation of beta-lactoglobulin and its retinol binding
    • Dufour, E., Bertrand-Harb, C., Haertle, T., Reversible effects of medium dielectric constant on structural transformation of beta-lactoglobulin and its retinol binding. Biopolymers 1993, 33, 589-598.
    • (1993) Biopolymers , vol.33 , pp. 589-598
    • Dufour, E.1    Bertrand-Harb, C.2    Haertle, T.3
  • 40
    • 0033778182 scopus 로고    scopus 로고
    • New insight on beta-lactoglobulin binding sites by 1-anilinonaphthalene-8-sulfonate fluorescence decay
    • Collini, M., D'Alfonso, L., Baldini, G., New insight on beta-lactoglobulin binding sites by 1-anilinonaphthalene-8-sulfonate fluorescence decay. Protein Sci. 2000, 9, 1968-1974.
    • (2000) Protein Sci. , vol.9 , pp. 1968-1974
    • Collini, M.1    D'Alfonso, L.2    Baldini, G.3
  • 41
    • 0001256511 scopus 로고
    • Structure of synthetic polypeptides
    • Elliott, A., Ambrose, E. J., Structure of synthetic polypeptides. Nature 1950, 165, 921-922.
    • (1950) Nature , vol.165 , pp. 921-922
    • Elliott, A.1    Ambrose, E.J.2
  • 42
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • Krimm, S., Bandekar, J., Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Adv. Protein Chem. 1986, 38, 181-364.
    • (1986) Adv. Protein Chem. , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 43
    • 0024963566 scopus 로고
    • Structure of cytochrome b5 in solution by Fourier-transform infrared spectroscopy
    • Holloway, P. W., Mantsch, H. H., Structure of cytochrome b5 in solution by Fourier-transform infrared spectroscopy. Biochemistry 1989, 28, 931-935.
    • (1989) Biochemistry , vol.28 , pp. 931-935
    • Holloway, P.W.1    Mantsch, H.H.2
  • 44
    • 0001701660 scopus 로고    scopus 로고
    • The conformation of alpha-lactalbumin as a function of pH, heat treatment and adsorption at hydrophobic surfaces studied by FTIR
    • Fang, Y., Dalgleish, D. G., The conformation of alpha-lactalbumin as a function of pH, heat treatment and adsorption at hydrophobic surfaces studied by FTIR. Food Hydrocolloids 1998, 12, 121-126.
    • (1998) Food Hydrocolloids , vol.12 , pp. 121-126
    • Fang, Y.1    Dalgleish, D.G.2
  • 45
    • 0038761793 scopus 로고    scopus 로고
    • Structural and interaction properties of beta-lactoglobulin as studied by FTIR spectroscopy
    • Lefèvre, T., Subirade, M., Structural and interaction properties of beta-lactoglobulin as studied by FTIR spectroscopy. Int. J. Food Sci. Technol. 1999, 34, 419-428.
    • (1999) Int. J. Food Sci. Technol. , vol.34 , pp. 419-428
    • Lefèvre, T.1    Subirade, M.2
  • 46
    • 0019536747 scopus 로고
    • Infrared and laser-Raman spectroscopic studies of thermally-induced globular protein gels
    • Clark, A., Saunderson, D., Suggett, A., Infrared and laser-Raman spectroscopic studies of thermally-induced globular protein gels. Int. J. Pept. Protein Res. 1981, 17, 353-364.
    • (1981) Int. J. Pept. Protein Res. , vol.17 , pp. 353-364
    • Clark, A.1    Saunderson, D.2    Suggett, A.3
  • 47
    • 0031574012 scopus 로고    scopus 로고
    • Conformation of beta-lactoglobulin studied by FTIR: Effect of pH, temperature, and adsorption to the oil-water interface
    • Fang, Y., Dalgleish, D., Conformation of beta-lactoglobulin studied by FTIR: Effect of pH, temperature, and adsorption to the oil-water interface. J. Colloid Interface Sci. 1997, 196, 292.
    • (1997) J. Colloid Interface Sci. , vol.196 , pp. 292
    • Fang, Y.1    Dalgleish, D.2
  • 48
    • 34547947641 scopus 로고    scopus 로고
    • Conversion of non-fibrillar beta-sheet oligomers into amyloid fibrils in Alzheimer's disease amyloid peptide aggregation
    • Benseny-Cases, N., Cócera, M., Cladera, J., Conversion of non-fibrillar beta-sheet oligomers into amyloid fibrils in Alzheimer's disease amyloid peptide aggregation. Biochem. Biophys. Res. Commun. 2007, 361, 916-921.
    • (2007) Biochem. Biophys. Res. Commun. , vol.361 , pp. 916-921
    • Benseny-Cases, N.1    Cócera, M.2    Cladera, J.3
  • 49
    • 0028804827 scopus 로고
    • Structural model for the beta-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide
    • Lansbury, P., Costa, P., Griffiths, J., Simon, E. et al., Structural model for the beta-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide. Nat. Struct. Mol. Biol. 1995, 2, 990-998.
    • (1995) Nat. Struct. Mol. Biol. , vol.2 , pp. 990-998
    • Lansbury, P.1    Costa, P.2    Griffiths, J.3    Simon, E.4
  • 50
    • 0035997080 scopus 로고    scopus 로고
    • Supramolecular structure in full-length Alzheimer's beta-amyloid fibrils: Evidence for a parallel beta-sheet organization from solid-state nuclear magnetic resonance
    • Balbach, J., Petkova, A., Oyler, N., Antzutkin, O. et al., Supramolecular structure in full-length Alzheimer's beta-amyloid fibrils: Evidence for a parallel beta-sheet organization from solid-state nuclear magnetic resonance. Biophys. J. 2002, 83, 1205-1216.
    • (2002) Biophys. J. , vol.83 , pp. 1205-1216
    • Balbach, J.1    Petkova, A.2    Oyler, N.3    Antzutkin, O.4
  • 51
    • 0030088058 scopus 로고    scopus 로고
    • Effects of physicochemical factors on the secondary structure of beta-lactoglobulin
    • Boye, J., Ismail, A., Alli, I., Effects of physicochemical factors on the secondary structure of beta-lactoglobulin. J. Dairy Res. 1996, 63, 97-109.
    • (1996) J. Dairy Res. , vol.63 , pp. 97-109
    • Boye, J.1    Ismail, A.2    Alli, I.3
  • 52
    • 0030993642 scopus 로고    scopus 로고
    • Effect of temperature on the secondary structure of beta-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: A test of the molten globule hypothesis
    • Qi, X., Holt, C., McNulty, D., Clarke, D. et al., Effect of temperature on the secondary structure of beta-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: A test of the molten globule hypothesis. Biochem. J. 1997, 324, 341.
    • (1997) Biochem. J. , vol.324 , pp. 341
    • Qi, X.1    Holt, C.2    McNulty, D.3    Clarke, D.4
  • 53
    • 0001744217 scopus 로고    scopus 로고
    • Use of differential scanning calorimetry and infrared spectroscopy in the study of thermal and structural stability of alpha-lactalbumin
    • Boye, J. I., Alli, I., Ismail, A. A., Use of differential scanning calorimetry and infrared spectroscopy in the study of thermal and structural stability of alpha-lactalbumin. J. Agric. Food Chem. 1997, 45, 1116-1125.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 1116-1125
    • Boye, J.I.1    Alli, I.2    Ismail, A.A.3
  • 54
    • 0029944773 scopus 로고    scopus 로고
    • Partially folded structure of monomeric bovine beta-lactoglobulin
    • Molinari, H., Ragona, L., Varani, L., Musco, G. et al., Partially folded structure of monomeric bovine beta-lactoglobulin. FEBS Lett. 1996, 381, 237.
    • (1996) FEBS Lett. , vol.381 , pp. 237
    • Molinari, H.1    Ragona, L.2    Varani, L.3    Musco, G.4
  • 55
    • 79956211956 scopus 로고    scopus 로고
    • The toxicity of bovine α-lactalbumin made lethal to tumor cells is highly dependent on oleic acid and induces killing in cancer cell lines and noncancer-derived primary cells
    • Brinkmann, C. R., Heegaard, C. W., Petersen, T. E., Jensenius, J. C., Thiel, S., The toxicity of bovine α-lactalbumin made lethal to tumor cells is highly dependent on oleic acid and induces killing in cancer cell lines and noncancer-derived primary cells. FEBS J. 2011, 278, 1955-1967.
    • (2011) FEBS J. , vol.278 , pp. 1955-1967
    • Brinkmann, C.R.1    Heegaard, C.W.2    Petersen, T.E.3    Jensenius, J.C.4    Thiel, S.5
  • 56
    • 79960844954 scopus 로고    scopus 로고
    • A novel method for preparation of HAMLET-like protein complexes
    • DOI: 10.1016/j.biochi.2011.1005.1002.
    • Permyakov, S. E., Knyazeva, E. L., Leonteva, M. V., Fadeev, R. S. et al., A novel method for preparation of HAMLET-like protein complexes. Biochimie 2011, DOI: 10.1016/j.biochi.2011.1005.1002.
    • (2011) Biochimie
    • Permyakov, S.E.1    Knyazeva, E.L.2    Leonteva, M.V.3    Fadeev, R.S.4
  • 57
    • 0031921236 scopus 로고    scopus 로고
    • Fatty acid transport: Difficult or easy
    • Hamilton, J. A., Fatty acid transport: Difficult or easy? J. Lipid Res. 1998, 39, 467-481.
    • (1998) J. Lipid Res. , vol.39 , pp. 467-481
    • Hamilton, J.A.1
  • 59
    • 0345704610 scopus 로고
    • Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor
    • Greene, L. A., Tischler, A. S., Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor. Proc. Natl. Acad. Sci. U. S. A. 1976, 73, 2424-2428.
    • (1976) Proc. Natl. Acad. Sci. U. S. A. , vol.73 , pp. 2424-2428
    • Greene, L.A.1    Tischler, A.S.2
  • 60
    • 0024550673 scopus 로고
    • Regulation of the differentiation of PC12 pheochromocytoma cells
    • Fujita, K., Lazarovici, P., Guroff, G., Regulation of the differentiation of PC12 pheochromocytoma cells. Environ. Health Perspect. 1989, 80, 127.
    • (1989) Environ. Health Perspect. , vol.80 , pp. 127
    • Fujita, K.1    Lazarovici, P.2    Guroff, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.